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Kurt Lang

Researcher at Roche Diagnostics

Publications -  45
Citations -  2994

Kurt Lang is an academic researcher from Roche Diagnostics. The author has contributed to research in topics: Amino acid & Peptide sequence. The author has an hindex of 17, co-authored 44 publications receiving 2941 citations. Previous affiliations of Kurt Lang include University of Regensburg & Hoffmann-La Roche.

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Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins.

TL;DR: The results indicate that this enzyme is probably identical to cyclophilin, a recently discovered mammalian protein which binds tightly to cyclosporin A (CsA), which is thought to be linked to the immunosuppressive action of CsA.
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Catalysis of protein folding by prolyl isomerase.

TL;DR: The enzyme peptidyl-prolyl cis-trans isomerase (PPIase) was discovered and purified from pig kidney and it is shown that it also catalyses slow steps in the refolding of a number of proteins of which fast- and slow-folding species have been observed and where it was suggested that proline isomerization was involved in slow refolding.
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Studies on the Mechanisms by Which Insulin-like Growth Factor (IGF) Binding Protein-4 (IGFBP-4) and IGFBP-5 Modulate IGF Actions in Bone Cells

TL;DR: IGBP-5 may in part stimulate bone cell proliferation by an IGF-independent mechanism involving IGF BP-5-specific cell surface binding sites independent of IGF receptors, according to studies on the mechanism by which IGFBP- 5 increased the binding of I-IGF tracer to bone cells.
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Structure of the IGF-binding domain of the insulin-like growth factor-binding protein-5 (IGFBP-5): implications for IGF and IGF-I receptor interactions.

TL;DR: It is shown that IGFBP‐5 inhibits the binding of IGFs to the IGF‐I receptor, resulting in reduction of receptor stimulation and autophosphorylation, and that the smaller N‐terminal fragments were less efficient inhibitors of the IGF-I receptor binding of insulin‐like growth factors.
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Molecular Cloning, Sequence, Expression, and Processing of the Interleukin 16 Precursor

TL;DR: It is reported here that pro-IL-16 is most likely synthesized as a 67-kDa protein and is encoded from a major 2.6-kb transcript, underlining the potential of IL-16 as an immune regulatory molecule.